ERH (gene)
In molecular biology, Enhancer of rudimentary homolog is a protein that in humans is encoded by the ERH gene.[3][4][5]
The Drosophila protein enhancer of rudimentary protein is a small protein of 104 amino acids. It has been found to be an enhancer of the rudimentary gene, involved in pyrimidine biosynthesis.[6]
From an evolutionary point of view, enhancer of rudimentary is highly conserved and has been found to exist in probably all multicellular eukaryotic organisms.[4] It has been proposed that this protein plays a role in the cell cycle.
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Isomura M, Okui K, Fujiwara T, Shin S, Nakamura Y (Sep 1996). "Cloning and mapping of a novel human cDNA homologous to DROER, the enhancer of the Drosophila melanogaster rudimentary gene". Genomics. 32 (1): 125–7. doi:10.1006/geno.1996.0086. PMID 8786099.
- 1 2 Gelsthorpe M, Pulumati M, McCallum C, Dang-Vu K, Tsubota SI (Apr 1997). "The putative cell cycle gene, enhancer of rudimentary, encodes a highly conserved protein found in plants and animals". Gene. 186 (2): 189–95. doi:10.1016/S0378-1119(96)00701-9. PMID 9074495.
- ↑ "Entrez Gene: ERH enhancer of rudimentary homolog (Drosophila)".
- ↑ Wojcik, E.; Murphy, A. M.; Fares, H.; Dang-Vu, K.; Tsubota, S. I. (1994). "Enhancer of rudimentaryp1, e(r)p1, a highly conserved enhancer of the rudimentary gene". Genetics. 138 (4): 1163–1170. PMC 1206255
. PMID 7896098.
Further reading
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Amente S, Napolitano G, Licciardo P, et al. (2005). "Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation". FEBS Lett. 579 (3): 683–9. doi:10.1016/j.febslet.2004.12.045. PMID 15670829.
- Wan C, Tempel W, Liu ZJ, et al. (2005). "Structure of the conserved transcriptional repressor enhancer of rudimentary homolog". Biochemistry. 44 (13): 5017–23. doi:10.1021/bi047785w. PMID 15794639.
- Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- Jin T, Guo F, Serebriiskii IG, et al. (2007). "A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks". Proteins. 68 (2): 427–37. doi:10.1002/prot.21343. PMID 17444515.
PDB gallery |
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| 1w9g: STRUCTURE OF ERH (ENHENCER OF RUDIMENTARY GENE) |
| 1wwq: Solution Structure of Mouse ER |
| 1wz7: Crystal structure of enhancer of rudimentary homologue (ERH) |
| 2nml: Crystal structure of HEF2/ERH at 1.55 A resolution |
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This article incorporates text from the public domain Pfam and InterPro IPR000781
